GenomeNet

Database: UniProt
Entry: S5RSF3_RHIET
LinkDB: S5RSF3_RHIET
Original site: S5RSF3_RHIET 
ID   S5RSF3_RHIET            Unreviewed;       318 AA.
AC   S5RSF3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN   ECO:0000313|EMBL:AGS20743.1};
GN   ORFNames=REMIM1_CH00895 {ECO:0000313|EMBL:AGS20743.1};
OS   Rhizobium etli bv. mimosae str. Mim1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1328306 {ECO:0000313|EMBL:AGS20743.1, ECO:0000313|Proteomes:UP000015261};
RN   [1] {ECO:0000313|EMBL:AGS20743.1, ECO:0000313|Proteomes:UP000015261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mim1 {ECO:0000313|EMBL:AGS20743.1,
RC   ECO:0000313|Proteomes:UP000015261};
RA   Rogel M.A., Bustos P., Santamaria R.I., Gonzalez V., Romero D.,
RA   Cevallos M.A., Lozano L., Ormeno-Orrillo E., Martinez-Romero E.;
RT   "Genomic basis of Rhizobium etli symbiovar mimosae and its prevalence among
RT   Phaseolus vulgaris nodule bacteria.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP005950; AGS20743.1; -; Genomic_DNA.
DR   RefSeq; WP_020920538.1; NC_021905.1.
DR   AlphaFoldDB; S5RSF3; -.
DR   KEGG; rel:REMIM1_CH00895; -.
DR   PATRIC; fig|1328306.3.peg.918; -.
DR   HOGENOM; CLU_057066_1_0_5; -.
DR   Proteomes; UP000015261; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   NCBIfam; TIGR00388; glyQ; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00254};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00254};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00254}.
SQ   SEQUENCE   318 AA;  35788 MW;  07A53ADFB9615112 CRC64;
     MSAIPDHMNP KRSFQALILT LHSYWADKGC AVLQPYDMEV GAGTFHPATT LRALGPKPWK
     AAYVQPSRRP SDGRYGENPN RLQHYYQYQV ILKPNPPNLQ ELYLGSLAAI CLDPLLHDIR
     FVEDDWESPT LGAWGLGWEC WCDGMEVSQF TYFQQVCGIE CAPVAGELTY GLERLAMYVQ
     GVDNVYDLNF NGREGDEKIS YGDVFLQAEQ EYSRNNFEFA NTEMLHRHFV DAEKECRSLL
     DAGAPDDSAN QRLHKCVFPA YDQCIKASHV FNLLDARGVI SVTERQSYIL RVRTLAKACG
     EAFLLTDAGG VNLSKEAA
//
DBGET integrated database retrieval system